Evidence for the presence and structure of asparagine-linked oligosaccharide units in the core protein of proteodermatan sulphate

Shinkai, Hiroshi; Nakamura, Takashi; Matsunaga, Etsuji

doi:10.1042/bj2130297

Cited by 17 publications

(3 citation statements)

References 19 publications

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“…The length of this chain also shows tissue variations from Mr 15000 to 45000 [144,239]. The skin PG has three 0-linked oligosaccharides [144] and one complex-type asparagine-linked oligosaccharide [213] per molecule. The amino acid composition of the core protein is quite different from that of the large aggregating cartilage PG.…”

Section: G1omerul Ar Basement Membranementioning

confidence: 99%

Proteoglycans in health and disease: structures and functions

Poole¹

1986

Biochemical Journal

435

197

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Section: G1omerul Ar Basement Membranementioning

confidence: 99%

Proteoglycans in health and disease: structures and functions

Poole¹

1986

Biochemical Journal

435

197

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“…The same complex-type oligosaccharide chain has also been found in proteodermatan sulphate from newborn-calf skin (Shinkai et al, 1983). Since the present studies were limited to the glycopeptidasereleasable oligosaccharides, it is uncertain whether oligosaccharide chains from the peptides.…”

Section: Discussionmentioning

confidence: 58%

The core molecule from type H proteoglycan. Release of mannose-containing oligosaccharides by digestion with N-oligosaccharide glycopeptidase

Takahashi¹,

Ishihara²,

Tejima³

et al. 1985

Biochemical Journal

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Chick-embryo cartilage contains a unique set of proteoglycans. Type H proteoglycan (PG-H) is the most abundant, constituting over 90% of the total cartilage hexuronate. We previously showed that treatment of PG-H with chondroitinase ACII and keratanase yields a protein-enriched core molecule [PG(-CS,KS)] with enzymically modified linkage oligosaccharides of the chondroitin sulphate and keratan sulphate chains. We report here that further treatment of PG(-CS,KS) with pepsin and N-oligosaccharide glycopeptidase (almond glycopeptidase) released four distinct types of mannose-containing oligosaccharide. Two of them were shown to be: (Formula: see text). Of the mannose-containing glycopeptides formed by pepsin digestion, about 40% (as mannose) were resistant to N-oligosaccharide glycopeptidase. Since the resistant fraction was enriched in keratan sulphate remnants, it is suggest that the mannose-containing oligosaccharides in this fraction represent those located in a keratan sulphate-enriched region of PG-H.

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“…This result indicated N -linked oligosaccharide chains; high mannose type or di -antennary complex type oligosaccharide chains bind to the core protein from proteodermatan sulfate. Proteodermatan sulfate as a major proteoglycan of calf skin had di-and tri-antennary complex type oligosaccharide chains in core protein Mr=55,000 (21). The functions of such Nlinked oligosaccharide chains on core protein are not known, but dermatan sulfate containing chondroitin sulfate rich proteoglycans which did not bind to concanavalin A Sepharose were recovered as major components of hypertrophic scar.…”

Section: Discussionmentioning

confidence: 99%

The Proteoglycans in Hypertrophic Scar

Honda

Matsunaga

Katagiri

et al. 1986

The Journal of Dermatology

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Sulfated proteoglycans of hypertrophic scar (6 months old after a burn) were extracted with 6 M hot urea, 0.02 M phosphate buffer, pH 7.0, containing protease inhibitors. Two types of proteoglycans, dermatan sulfate proteoglycans and chondroitinsulfate rich proteoglycans, were recovered. The dermatan sulfate proteoglycans, which are capable of binding to concanavalin A, were composed of Mr=53000 core protein and iduronate rich dermatan sulfate. The chondroitin sulfate rich proteoglycans did not bind to concanavalin A but had the same size core proteins as the dermatan sulfate proteoglycans, based on SDS‐polyacrylamide gel electrophoresis. The tryptic peptide mappings showed that the core proteins from dermatan sulfate have the same structural sequences as those from chondroitin sulfate rich proteoglycans.

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Evidence for the presence and structure of asparagine-linked oligosaccharide units in the core protein of proteodermatan sulphate

Cited by 17 publications

References 19 publications

Proteoglycans in health and disease: structures and functions

Proteoglycans in health and disease: structures and functions

The core molecule from type H proteoglycan. Release of mannose-containing oligosaccharides by digestion with N-oligosaccharide glycopeptidase

The Proteoglycans in Hypertrophic Scar

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